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Literature summary for 7.4.2.5 extracted from

  • Robson, A.; Carr, B.; Sessions, R.B.; Collinson, I.
    Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complex (2009), FEBS Lett., 583, 207-212.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in a SecA-overproducing Escherichia coli strain Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ 2 mM Mg2+ blocks SecA ATPase activity almost completely, the inhibition is abolishable by binding of SecA to the protein channel SecYEG in proteoliposomes (1 micromol) Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
ATP
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
425 mol ATP/min/mol SecA in presence of 0.2 micromol preprotein translocation substrate proOmpA in urea Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
SecA
-
Escherichia coli